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Protein struct/funct

Bio 2 Lecture 2

QuestionAnswer
What is the most abundant organic compound in our body? Proteins
What are the 7 functions of proteins? 1-Structural 2-Catalysts 3-Movement 4-Transport 5-Defence 6-Regulation 7-Storage
[Functions] What are the characteristics of the structural function? Give example Construct different structures, provide scaffolding for cell shape. Ex: collagen in tendons, cytoskeleton
[Functions] What are the characteristics of the catalyst function? Give example Enzymes used to kick-start biochemical reaction. Enzymes are like maltase or lactase
[Functions] What are the characteristics of the movement function? Give example Contractile motion of protein moves muscle (so protein are walking, recall infamous video)
[Functions] What are the characteristics of the transport function? Give example Carry substances in the blood or lymph throughout the body. It's a fixed protein that carries thing. Ex: hemoglobin for oxygen transport, trasnferrin for iron transport
[Functions] What are the characteristics of the defence function? Give example Protect the body from foreign pathogens/harmful substances. Ex: antibodies
[Functions] What are the characteristics of the regulation function? Give example Turn off and on processes. Ex: Insulin regulates sugar going into a cell
[Functions] What are the characteristics of the storage function? Give example Stores lol. Example: Storage of iron in toxic-free vesicles
Where do protein come from? The Central Dogma
What dictates the final shape of the protein and the sequential order of amino acids? Our genes. DNA--»RNA--»Protein--» One of the 7 functions depending on the shape (which is determined by the 4 structural levels)
What is the process of protein synthesis? See notes, but basically: DNA--»RNA--»Protein
What do you build when you link amino acids? protein
What is a protein building block? What atoms are associated with AA's? an amino acid, SNOCH atoms
Are the 20 AA's found in every living thing? Yes
[Chemical properties of AA] What kind of bonds can non-polar AA's form? Hydrophobic bonds
[Chemical properties of AA] What kind of bonds can polar AA's form? Hydrogen bonds (H-bonds)
[Chemical properties of AA] What kind of bonds can charged AA's form? Ionic bonds
[Chemical properties of AA] What kind of bonds can special AA's form? Disulfied Bridge, aka covalent bonds
What is the backbone of an AA made out off? A carboxylix acid group, a amino group, a hydrogen attached to the central carbon. Each AA have the same backbone
What differs from AA to AA? The R-group
[Organization Level] What is a primary protein organization level? What are the bonds here? The order of the amino acids in the protein is called the primary structure of the protein. The chain of polypeptide are made out of amino acids linked by peptide bonds. Primary gives peptide bonds.
Which terminus has the amino acid group? The N-terminal
Which terminus has the carboxylic acid group? The C-terminal
With which terminal does a protein sequence start and ends? What are the charges of each? It starts with the N-terminal and ends with the C-terminal. N-terminal is positively charged and C-terminal is negatively charged.
[Organization Level] What is a secondary protein organization level? What are the bonds here? It's the folding of the polypeptide. Can form aalpha helix or a beta pleated sheet. Causes H-bonds
[Organization Level] What is a tertiary protein organization level? What are the bonds here? Sidechain bonds fold one polypeptide. The R-groups must be facing eachother (like in the lab). Can be beta sheet, alpha helix or random coils. Bonds are ionic bonds- polar H-bonds - Van der Waals forces - disulfide bridge -hydrophobic exclusion
[Organization Level] What is a quaternary protein organization level? What are the bonds here? Sidechain bonds associate with two or more polypeptides holding them together. The possible bonds are ionic bonds- H-bonds - Van der Waals forces - disulfide bridge
What does a peptide bond link? 2 amino acids
How are the 2 secondary shapes formed? The oxygen of the carbonyl group and the hydrogen of the amino group in the backbone form Hydrogen bonds. This creates 2 shapes: Alpha helix and beta pleated sheet
Where is the bond for alpha helix? A H-bond every 2 to 4 amino acids, see image
Where is the bond for beta plates sheet? between strands, see image (different chains of polypeptide connect to eachother either in a parallel manner, anti-parallel or mixed so both parallel and anti-p )
Whats the difference between secondary and tertiary organization? The shape, secondary has either beta pleated sheet or alpha helix, while tertiary is the overall 3D shape that is globular and might include beta pleated and alpha helix and random coils.
What are the 2 possible overall shapes of a quaternary structure? Either fibrous or globular. Fibrous tend to be for structural proteins like microtubules while globular proteins are for other functions like enzymes and hemoglobin (so catalyst and transport)
What are 2 structural characteristics? Motifs and domains. Motif are common elements of repeating secondary structure (like a barrel shape). Domains are characteristic functional units within a larger structure (like pieces of an engine)(ex: portion of the protein that spins)
What are the different kinds of biological macromolecules? There's carbohydrates, proteins, nucleic acids and lipids.
How is the central dogma related to proteins? Replication, Transcription, and Translation are the 3 main processes used by all cells to maintain their genetic information and to convert the genetic information encoded in DNA into gene products, which are either RNAs or proteins
What is the central dogma? The central dogma describes the flow of genetic information from DNA to RNA to protein.
What are the different classes of protein? They're grouped by functions, so there's catalyzing proteins.., structure, movement, transport, storage, regulation, defense,
Draw a general amino acid and then link it to another amino acid
Go ask the questions in the PPW comments
Created by: Malayka
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